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Giulio Fermi's Contributions to Biophysics and Molecular Biology

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Giulio Fermi's Contributions to Biophysics and Molecular Biology Giulio Fermi’s contributions to biophysics and molecular biology Fabio Pichierri Department of Applied Chemistry, Graduate School of Engineering, Tohoku University, Aoba-yama 6-6-07, Sendai 980-8579, Japan E-mail address: [email protected] [v.1, January 7, 2018] Abstract This paper presents a comprehensive list of the scientific articles of Giulio Fermi (1936-1997), son of the Italian-American physicist Enrico Fermi, published between 1962 and 1997. The initial research activity of Giulio was concerned with virology and biological cybernetics while, from 1975 onward, his work was completely devoted to protein crystallography. The crystallographic research was carried out in collaboration with Nobel laureate Max Perutz at the Medical Research Council (MRC) Laboratory of Molecular Biology in Cambridge (United Kingdom). A short biography of Giulio (Judd) Fermi appears inside John Finch’s book “A Nobel Fellow on Every Floor: A History of the Medical Research Council Laboratory of Molecular Biology” published by the MRC in 2008. Keywords: History of Science; Virology; Biological Cybernetics; Biocrystallography; Hemoglobin; Protein Structure; Biomolecules 1 1. Introduction Enrico Fermi (1901-1954) [1-6], the famous Italian-American physicist who displayed the rare ability of performing both experimental and theoretical research at equal levels of originality and creativity, received the Nobel Prize for Physics in 1938 "for his demonstrations of the existence of new radioactive elements produced by neutron irradiation, and for his related discovery of nuclear reactions brought about by slow neutrons" [7]. When the award ceremonies in Stockholm were over, after paying a short visit to Niels Bohr in Copenhagen, Enrico and his family fled to America on board of the RMS Franconia [3]. Once arrived in New York, Enrico told his wife Laura (1907- 1977) that they had thus established the American branch of the Fermis [1]. Along with his wife there were two children, daughter Nella (1931-1995) and son Giulio (1936 -1997). Giulio, named in honor of Enrico’s elder brother who passed away in 1915 while he was still a teenager, was initially attracted to mathematics (Master of Arts at Princeton University in 1957) but eventually studied biophysics and molecular biology at the University of California, Berkely, obtaining a Ph. D in 1961 under the guidance of Gunther S. Stent (1924-2008) [8]. After a postdoc in Europe at the Max Planck Institute (MPI) for Biology (now MPI for Biological Cybernetics) in Tubingen with Werner E. Reichardt (1924-1992) and a brief parenthesis as system analyst back in the United States, in 1971 Giulio joined the Medical Research Council Laboratory of Molecular Biology (MRC-LMB) in Cambridge (UK) under the wing of Nobel laureate Max Perutz (1914-2002) [9]. Here he performed research work on the structure and function of proteins, particularly on hemoglobin (Hb), the 2 oxygen transporter found on the red blood cells of vertebrates [8]. Giulio (co)authored several scientific papers (vide infra) in the Journal of Molecular Biology (JMB) as well as in other biological or biochemical journals. After more than twenty years since Giulio’s death, I decided to collect his scientific papers in a list which provides an overview of his scientific ouvre. The majority of scientific publications in the list below (section 3) are available on-line in the corresponding journals’ home-pages. To the best of my knowledge, apart for a short biography that appears inside John Finch’s book [8], the scientific contributions of Giulio (Judd) Fermi have not been as yet summarized. 2. Methods The Web of Science database [10] was accessed several times throughout 2017. To avoid confusion with the papers listed in the reference list placed at the end of this manuscript, Giulio Fermi’s papers are numbered with Roman numerals. Along with the journal papers the list also comprises a paper contributed for a book chapter (XXXI) and an Atlas coauthored with Max Perutz (VII). Hereafter follows the list of scientific publications of Giulio Fermi while section 4 provides some comments about the research results of selected papers. 3. Bibliography of Giulio Fermi I. G. Fermi, G.S. Stent, Protein Synthesis and the Onset of Intracellular Bacteriophage Growth ID. Replication of the Genome of a Secondary Phage, 3 J. Mol. Biol. 4 (1962)179-192. II. G. Fermi, G.S. Stent, Effects of Chloramphenicol and of Multiplicity of Infection on Induced Mutation in Bacteriophage T4, Zeitschrift fiir Vererbungslehre 93 (1962) 177-187. III. G. Fermi, W. Reichardt, Optomotorische Reaktionen der Fliege Musca domestica. Abhäingigkeit der Reaktion yon der WellenNinge, der Geschwindigkeit, dam Kontrast und der mittleren Leuehtdiehte bewegter periodischer Muster, , Kybernetik (1963) 15-28. IV. G. Fermi, Three-dimensional Fourier Synthesis of Human Deoxyhaemoglobin at 2.5 Å Resolution: Refinement of the Atomic Model, J. Mol. Biol. 97 (1975) 237-256. V. G. Fermi, M.F. Perutz, Structure of Human Fluoromethaemoglobin with Inositol Hexaphosphate J. Mol. Biol. 114 (1977) 421-431. VI. C. Messana, M. Cerdonio, P. Shenkin, R.W. Noble, G. Fermi, R.N. Perutz, M.F. Perutz, Influence of Quaternary Structure of the Globin on Thermal Spin Equilibria in Different Methemoglobin Derivatives, Biochemistry 17 (1978) 3652-3662. VII. G. Fermi, M.F. Perutz, Atlas of Molecular Structures in Biology: Volume 2. Haemoglobin and Myoglobin, Oxford University Press (1981). VIII. G. Fermi, M. Perutz, Structure of Human Deoxy Cobalt Haemoglobin, J. Mol. Biol. 155 (1982) 495-505. IX. G. Fermi, M. Perutz, B. Shaanan, R. Fourme, The Crystal Structure of Human Deoxyhaemoglobin at 1.74 Resolution, J. Mol. Biol. 175 (1984) 159- 174. 4 X. M.F. Perutz, G. Fermi, T.-B. Shih, Structure of deoxyhemoglobin Cowtown [His HC3(146),8-Leu]: Origin of the alkaline Bohr effect and electrostatic interactions in hemoglobin, Proc. Natl. Acad. Sci. USA 81 (1984) 4781-4784. XI. M.F. Perutz, G. Fermi, D.J. Abraham, C. Poyart, E. Bursaux, Hemoglobin as a Receptor of Drugs and Peptides: X-ray Studies of the Stereochemistry of Binding, J. Am. Chem. Soc. 108 (1986) 1064-1078. XII. M.F. Perutz, G. Fermi, R.G. Shulman, Iron distances in hemoglobin: Comparison of x-ray crystallographic and extended x-ray absorption fine structure studies, Proc. Natl. Acad. Sci. USA 84 (1987) 6167-6168. XIII. M.F. Perutz, G. Fermi, B. Luisi, B. Shaanan, R.C. Liddington, Stereochemistry of Cooperative Mechanisms in Hemoglobin, Cold Spring Harb. Symp. Quant. Biol. 52 (1987) 555-565. XIV. M.F. Perutz, G. Fermi, B. Luisi, B. Shaanan, R.C. Liddington, Stereochemistry of Cooperative Mechanisms in Hemoglobin, Acc. Chem. Res. 20 (1987) 309-321. XV. M. Perutz, G. Fermi, J. Fogg, S. Rahbar, Indirect Allosteric Effects of a Neutral Mutation: Structure of Deoxyhaemoglobin North Chicago (ProC2(36)Ser), J. Mol. Biol. 201 (1988) 459-461. XVI. I. Lalezari, S. Rahbar, P. Lalezari, G. Fermi, M. Perutz, LR16, a compound with potent effects on the oxygen affinity of hemoglobin, on blood cholesterol, and on low density lipoprotein, Proc. Natl. Acad. Sci. USA 85 (1988) 6117-6121. XVII. K. Nagai, D. Altschuh, G. Fermi, Structure, Function and Evolution of Hemoglobin Studied by Protein Engineering and X-ray Crystallography, 5 Biological Chemistry Hoppe-Seyler, 369 (1988) 204-204. XVIII. M.F. Perutz, G. Fermi, Stereochemistry of salt-bridge formation in α- helices and β-strands, Proteins: Structure, Function, and Bioinformatics, 4 (1988) 294-295. XIX. M.P. Kavanaugh, M.F Perutz, G. Fermi, D.T. Shih, R.T. Jones, Structure and Function of Human Hemoglobin Covalently Labeled with Periodate- oxidized Adenosine Triphosphate, J. Biol. Chem. 264 (1989) 11009-11013. XX. B. Luisi, B. Liddington, G. Fermi, N. Shibayama, Structure of Deoxy- quaternary Haemoglobin with Liganded Subunits, J. Mol. Biol. 214 (1990) 1-14. XXI. I. Lalezari, P. Lalezari, C. Poyart, M. Marden, J. Kister, B. Bohn, G. Fermi, M. F. Perutz, New Effectors of Human Hemoglobin: Structure and Function, Biochemistry 29 (1990) 1515-1523. XXII. Y. Huang, J. Pagnier, P. Magne, F. Baklouti, J. Kister, J. Delaunay, C. Poyart, G. Fermi, M.F. Perutz, Structure and Function of Hemoglobin Variants at an Internal Hydrophobic Site: Consequences of Mutations at the 27 (B9) Position, Biochemistry 29 (1990) 7020-7023. XXIII. G.R. Honig, L.N. Vida, B.B. Rosenblum, M.F. Perutz, G. Fermi, Hemoglobin Warsaw (Phe42(CD1) Val), an Unstable Variant with Decreased Oxygen Affinity, J. Biol. Chem. 265 (1990) 126-132. XXIV. C. Bonaventura, R. Cashon, J. Bonaventura, M. Perutz, G. Fermi, D.T.- B. Shih, Involvement of the Distal Histidine in the Low Affinity Exhibited by Hb Chico (Lys Thr) and Its Isolated Chains, J. Biol. Chem. 266 (1991) 23033-23040. 6 XXV. T.-H. Jessen, R.E. Weber, G. Fermi, J. Tame, G. Braunitzer, Adaptation of bird hemoglobins to high altitudes: Demonstration of molecular mechanism by protein engineering, Proc. Natl. Acad. USA 88 (1991) 6519-6522. XXVI. J. Tame, D.T.-B. Shih, J. Pagnier, G. Fermi, K. Nagai, Functional Role of the Distal Valine (E11) Residue of Subunits in Human Haemoglobin, J. Mol. Biol. 218 (1991) 761-767. XXVII. L. Camardella, C. Caruso, R. D’Avino, G. di Prisco, B. Rutigliano, M. Tamburrini, G. Fermi, M.F. Perutz, Haemoglobin of the Antarctic Fish Pagothenia bernacchii: Amino Acid Sequence, Oxygen Equilibria and Crystal Structure of Its Carbonmonoxy Derivative, J. Mol. Biol. 224 (1992) 449-460. XXVIII. G. Fermi, M.F. Perutz, D. Williamson, P. Stein, D.T-b. Shih, Structure-Function Relationships in the Low-affinity Mutant Haemoglobin Aalborg (Gly74 (E18)Arg), J. Mol. Biol. 226 (1992) 883-888. XXIX. D. Looker, D. Abbott-Brown, P. Cozart, S. Durfee, S. Hoffman, A.J. Mathews, J. Miller-Roehrkh, S. Shoemaker, S. Trimble, G. Fermi, N.H. Komiyama, K. Nagai, G.L. Stetler, A human recombinant haemoglobin designed for use as a blood substitute, Nature 356 (1992) 258-260.
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